ArticleMethods in molecular biology (Clifton, N.J.)2026
Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The complexity of biological samples often necessitates specialized processing and instrumentation to enable the assessment of disease-associated biomarkers, highlighting the need for simple and robust methods of multiplex detection. Nanopore biosensors represent a promising technology to address this challenge, with biological nanopores emerging as versatile scaffolds for sensor development. In particular, monomeric outer membrane proteins (OMPs) provide an accessible platform for site-specific engineering with reproducible, atomically precise fabrication. Outer membrane protein G (OmpG), a monomeric Escherichia coli porin possessing seven flexible extracellular loops that can be functionalized with affinity ligands, has been utilized as a highly selective sensor through a distinctive gating-pattern detection mode arising from loop-mediated sampling of the molecular surface of bound analytes. Here, we present a general protocol for the molecular grafting of two peptide affinity motifs onto OmpG, followed by purification and characterization of the engineered construct, to generate a single-channel multiplex sensor.
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